View source for 9kts


==Structure of TauT in the apo state==
<StructureSection load='9kts' size='340' side='right'caption='[[9kts]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9kts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9KTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9KTS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9kts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9kts OCA], [https://pdbe.org/9kts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9kts RCSB], [https://www.ebi.ac.uk/pdbsum/9kts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9kts ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/SC6A6_HUMAN SC6A6_HUMAN] The disease is caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/SC6A6_HUMAN SC6A6_HUMAN] Mediates sodium- and chloride-dependent transport of taurine (PubMed:31345061, PubMed:31903486, PubMed:8010975, PubMed:8382624, PubMed:8654117). Mediates transport of beta-alanine (PubMed:8010975). Can also mediate transport of hypotaurine and gamma-aminobutyric acid (GABA) (By similarity).[UniProtKB:O35316]<ref>PMID:31345061</ref> <ref>PMID:31903486</ref> <ref>PMID:8010975</ref> <ref>PMID:8382624</ref> <ref>PMID:8654117</ref>   Sodium-dependent taurine and beta-alanine transporter. Chloride ions are necessary for optimal uptake.<ref>PMID:31345061</ref> <ref>PMID:31903486</ref> <ref>PMID:8382624</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Taurine, a sulfur-containing amino acid, is vital for human health because of its antioxidant, anti-inflammatory, and osmoregulatory properties. Its homeostasis is maintained by the Na(+)/Cl(-)-dependent taurine transporter (TauT). Here, we present five atomic structures of human TauT: apo, taurine bound, and complexes with three taurine-mimetic inhibitors, including beta-alanine, gamma-aminobutyric acid (GABA), and guanidinoethyl sulfonate (GES). The structures of taurine-, beta-alanine-, and GABA-bound human TauT (hTauT) in complex with NaCl adopt an occluded conformation, with ligands binding in a central pocket. With KCl, GES-bound hTauT adopts an inward-facing conformation, with two GES positioned along the substrate translocation pathway in a bipartite manner: one in the deep central cavity and the other precluding structural transition to the occluded state. The radioactive taurine uptake analyses clearly demonstrate the impact of residues on taurine recognition and inhibitor selection. These structures provide insights into the overall architecture, substrate coordination, and inhibitor recognition mechanism of TauT.

Structural determination of the human taurine transporter TauT reveals the mechanism of substrate and inhibitor recognition.,Lu Y, Ding D, Chen H, Jiang P, Luo J, Shan H, Wang G, Luo J, Yin Y Cell Rep. 2025 Nov 19;44(12):116591. doi: 10.1016/j.celrep.2025.116591. PMID:41269860<ref>PMID:41269860</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9kts" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ding D]]
[[Category: Lu YS]]
[[Category: Yin YX]]